Cited by 1,518Advanced Glycation End Products researchChronic Kidney Disease and DiabetesRetinal Diseases and Treatments

Advanced Glycation End Products and Diabetic Complications

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Singh, Varun Parkash, Bali, Anjana, Singh, Nirmal, Jaggi, Amteshwar Singh·2014·The Korean Journal of Physiology & Pharmacology

Abstract

During long standing hyperglycaemic state in diabetes mellitus, glucose forms covalent adducts with the plasma proteins through a non-enzymatic process known as glycation. Protein glycation and formation of advanced glycation end products (AGEs) play an important role in the pathogenesis of diabetic complications like retinopathy, nephropathy, neuropathy, cardiomyopathy along with some other diseases such as rheumatoid arthritis, osteoporosis and aging. Glycation of proteins interferes with their normal functions by disrupting molecular conformation, altering enzymatic activity, and interfering with receptor functioning. AGEs form intra- and extracellular cross linking not only with proteins, but with some other endogenous key molecules including lipids and nucleic acids to contribute in the development of diabetic complications. Recent studies suggest that AGEs interact with plasma membrane localized receptors for AGEs (RAGE) to alter intracellular signaling, gene expression, release of pro-inflammatory molecules and free radicals. The present review discusses the glycation of plasma proteins such as albumin, fibrinogen, globulins and collagen to form different types of AGEs. Furthermore, the role of AGEs in the pathogenesis of diabetic complications including retinopathy, cataract, neuropathy, nephropathy and cardiomyopathy is also discussed.

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Crossref · 10.4196/kjpp.2014.18.1.1

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  1. [73]Hofmann MA Drury S Fu C Qu W Taguchi A Lu Y Avila C Kambham N Bierhaus A Nawroth P Neurath MF Slattery T Beach D McClary J Nagashima M Morser J Stern D Schmidt AM RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides Cell 1999 97 889 901 10399917

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Authors
Singh, V. P., Bali, A., Singh, N., & Jaggi, A. S.
Affiliations
Punjabi University (IN)
Corresponding author
Jaggi, Amteshwar Singh
Venue
The Korean Journal of Physiology & Pharmacology
Published
2014
Volume
18
Issue
1
Pages
1
ISSN
  • 1226-4512 (ISSN-L)
  • 2093-3827
OpenAlex
W2120293565
Cited by
1,518
References
187
Citations by year
2026: 109 · 2025: 144 · 2024: 146 · 2023: 144 · 2022: 185 · 2021: 159 · 2020: 174 · 2019: 119 · 2018: 117 · 2017: 96 · 2016: 70 · 2015: 36 · 2014: 18
FWCI
9.33
Type
journal article
Language
en
Open access
Locations
  • Korean Journal of Physiology and Pharmacology (publishedVersion, cc-by-nc)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
  • Health Sciences › Medicine › Nephrology › Chronic Kidney Disease and Diabetes
  • Health Sciences › Medicine › Ophthalmology › Retinal Diseases and Treatments
Keywords
advanced glycation end products, diabetes complications, glycation, protein glycation, receptor for advanced glycation end products, retinopathy, kidney disease, neuropathy, cardiomyopathy, cataract, albumin, fibrinogen, collagen, hyperglycemia, pro-inflammatory signaling, free radicals

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